ID A0P819_9PROT Unreviewed; 461 AA.
AC A0P819;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Peptidase S41A, protease {ECO:0000313|EMBL:EAV47679.1};
GN ORFNames=MB2181_06360 {ECO:0000313|EMBL:EAV47679.1};
OS Methylophilales bacterium HTCC2181.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales; OM43 clade.
OX NCBI_TaxID=383631 {ECO:0000313|EMBL:EAV47679.1, ECO:0000313|Proteomes:UP000054262};
RN [1] {ECO:0000313|EMBL:EAV47679.1, ECO:0000313|Proteomes:UP000054262}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2181 {ECO:0000313|EMBL:EAV47679.1,
RC ECO:0000313|Proteomes:UP000054262};
RA Giovannoni S., Vergin K., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAV47679.1}.
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DR EMBL; AAUX01000001; EAV47679.1; -; Genomic_DNA.
DR AlphaFoldDB; A0P819; -.
DR MEROPS; S41.004; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000054262; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00988; PDZ_CTP_protease; 1.
DR CDD; cd07560; Peptidase_S41_CPP; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.750.44; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR005151; Tail-specific_protease.
DR NCBIfam; TIGR00225; prc; 1.
DR PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004404};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:EAV47679.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054262};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}.
FT DOMAIN 89..157
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 401..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 461 AA; 50599 MW; 39CDF56DD3B28158 CRC64;
MRSKFEKVTL IFIGLFLGLL ISVNLPVFAD KTKSSELPIE DLRTFAEVFG KIKTDYVEVV
EDKKLLSEAL SGMLSGLDPH STYLDLDHFK DLQQGTAGEF GGLGIEVGME DGFVKVISPI
EDTPAYDAGL KSGDLIMKLD ETQVKGLGLN DAVKLMRGKP GTAINLQVLR KGVDTPINIK
IVRAQIKTKS VKSKMIEPNY GYVRVTQFQE RTGEDLAAAL QKLWKENKHP LNGLILDMRN
NPGGLLNSAV AVSAAFLNEG DLVVYTEGRA ADSKMHLTTI PENFIRNNPQ KNNYIKKLPK
DYKNTPLVVL VNNGSASASE IVAGALQDHK RALIVGTRSF GKGSVQSILP MNNGTAIKLT
TARYFTPNGR SIQAKGIDPD IIIEDGNESI PVMREADLTN RLSNPEEKEL APSEDQSKNK
PTSDGGEALR NYKPIELGGE DDKQYAEAIK ILKDIDRYQK N
//
